ID   HUTH_MOUSE              Reviewed;         657 AA.
AC   P35492;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   09-FEB-2010, entry version 78.
DE   RecName: Full=Histidine ammonia-lyase;
DE            Short=Histidase;
DE            EC=4.3.1.3;
GN   Name=Hal; Synonyms=Hsd, Huth;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT HIS GLN-322.
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RX   MEDLINE=93252384; PubMed=8486363; DOI=10.1006/geno.1993.1164;
RA   Taylor R.G., Grieco D., Clarke G.A., McInnes R.R., Taylor B.A.;
RT   "Identification of the mutation in murine histidinemia (his) and
RT   genetic mapping of the murine histidase locus (Hal) on chromosome
RT   10.";
RL   Genomics 16:231-240(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-648, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631; SER-635 AND
RP   SER-648, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635, AND MASS
RP   SPECTROMETRY.
RX   PubMed=18973353; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- CATALYTIC ACTIVITY: L-histidine = urocanate + NH(3).
CC   -!- PATHWAY: Amino-acid degradation; L-histidine degradation into L-
CC       glutamate; N-formimidoyl-L-glutamate from L-histidine: step 1/3.
CC   -!- PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO),
CC       which is formed autocatalytically by cyclization and dehydration
CC       of residues Ala-Ser-Gly (By similarity).
CC   -!- DISEASE: Defects in Hal are the cause of histidinemia (His).
CC   -!- SIMILARITY: Belongs to the PAL/histidase family.
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DR   EMBL; L07645; AAA37777.1; -; mRNA.
DR   EMBL; AK014518; BAB29407.1; -; mRNA.
DR   EMBL; BC057637; AAH57637.1; -; mRNA.
DR   IPI; IPI00118625; -.
DR   PIR; A46128; A46128.
DR   RefSeq; NP_034531.1; -.
DR   UniGene; Mm.13000; -.
DR   SMR; P35492; 3-83, 114-616.
DR   STRING; P35492; -.
DR   PhosphoSite; P35492; -.
DR   PRIDE; P35492; -.
DR   Ensembl; ENSMUST00000016031; ENSMUSP00000016031; ENSMUSG00000020017; Mus musculus.
DR   GeneID; 15109; -.
DR   KEGG; mmu:15109; -.
DR   NMPDR; fig|10090.3.peg.14273; -.
DR   UCSC; uc007gus.1; mouse.
DR   CTD; 15109; -.
DR   MGI; MGI:96010; Hal.
DR   eggNOG; roNOG12953; -.
DR   HOGENOM; HBG510887; -.
DR   HOVERGEN; P35492; -.
DR   InParanoid; P35492; -.
DR   OMA; QKGQIDS; -.
DR   OrthoDB; EOG97DD2R; -.
DR   BRENDA; 4.3.1.3; 244.
DR   NextBio; 287506; -.
DR   ArrayExpress; P35492; -.
DR   Bgee; P35492; -.
DR   CleanEx; MM_HAL; -.
DR   Genevestigator; P35492; -.
DR   GermOnline; ENSMUSG00000020017; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005625; C:soluble fraction; IDA:MGI.
DR   GO; GO:0016211; F:ammonia ligase activity; IEA:InterPro.
DR   GO; GO:0004397; F:histidine ammonia-lyase activity; IDA:MGI.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0006548; P:histidine catabolic process; IDA:MGI.
DR   InterPro; IPR005921; HutH.
DR   InterPro; IPR008948; L-Aspartase-like.
DR   InterPro; IPR001106; Phe/His_NH3-lyase.
DR   Pfam; PF00221; PAL; 1.
DR   TIGRFAMs; TIGR01225; hutH; 1.
DR   PROSITE; PS00488; PAL_HISTIDASE; 1.
PE   1: Evidence at protein level;
KW   Disease mutation; Histidine metabolism; Lyase; Phosphoprotein.
FT   CHAIN         1    657       Histidine ammonia-lyase.
FT                                /FTId=PRO_0000161059.
FT   MOD_RES     254    254       2,3-didehydroalanine (Ser) (By
FT                                similarity).
FT   MOD_RES     631    631       Phosphoserine.
FT   MOD_RES     635    635       Phosphoserine.
FT   MOD_RES     648    648       Phosphoserine.
FT   CROSSLNK    253    255       5-imidazolinone (Ala-Gly) (By
FT                                similarity).
FT   VARIANT     322    322       R -> Q (in His; reduced stability).
SQ   SEQUENCE   657 AA;  72258 MW;  03402C348686C22D CRC64;
     MPRYTVHVRG EWLAVPCQDG KLTVGWLGRE AVRRYMKNKP DNGGFTSVDE VQFLVHRCKG
     LGLLDNEDEL EVALEDNEFV EVVIEGDVMS PDFIPSQPEG VFLYSKYREP EKYIALDGDS
     LSTEDLVNLG KGRYKIKLTS IAEKKVQQSR EVIDSIIKER TVVYGITTGF GKFARTVIPA
     NKLQELQVNL VRSHSSGVGK PLSPERCRML LALRINVLAK GYSGISLETL KQVIEAFNAS
     CLSYVPEKGT VGASGDLAPL SHLALGLIGE GKMWSPKSGW ADAKYVLEAH GLKPIVLKPK
     EGLALINGTQ MITSLGCEAL ERASAIARQA DIVAALTLEV LKGTTKAFDT DIHAVRPHRG
     QIEVAFRFRS LLDSDHHPSE IAESHRFCDR VQDAYTLRCC PQVHGVVNDT IAFVKDIITT
     ELNSATDNPM VFASRGETIS GGNFHGEYPA KALDYLAIGV HELAAISERR IERLCNPSLS
     ELPAFLVAEG GLNSGFMIAH CTAAALVSES KALCHPSSVD SLSTSAATED HVSMGGWAAR
     KALRVVEHVE QVLAIELLAA CQGIEFLRPL KTTTPLEKVY DLVRSVVRPW IKDRFMAPDI
     EAAHRLLLDQ KVWEVAAPYI EKYRMEHIPE SRPLSPTAFS LESLRKNSAT IPESDDL
//